EKI1_HUMAN
ID EKI1_HUMAN Reviewed; 452 AA.
AC Q9HBU6; G5E969;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ethanolamine kinase 1 {ECO:0000305};
DE Short=EKI 1 {ECO:0000303|PubMed:11044454};
DE EC=2.7.1.82;
GN Name=ETNK1 {ECO:0000312|HGNC:HGNC:24649};
GN Synonyms=EKI1 {ECO:0000303|PubMed:11044454};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11044454; DOI=10.1074/jbc.m008794200;
RA Lykidis A., Wang J., Karim M.A., Jackowski S.;
RT "Overexpression of a mammalian ethanolamine-specific kinase accelerates the
RT CDP-ethanolamine pathway.";
RL J. Biol. Chem. 276:2174-2179(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Highly specific for ethanolamine phosphorylation. May be a
CC rate-controlling step in phosphatidylethanolamine biosynthesis.
CC {ECO:0000269|PubMed:11044454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine;
CC Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216;
CC EC=2.7.1.82; Evidence={ECO:0000269|PubMed:11044454};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070;
CC Evidence={ECO:0000269|PubMed:11044454};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC {ECO:0000269|PubMed:11044454}.
CC -!- INTERACTION:
CC Q9HBU6; P49069: CAMLG; NbExp=3; IntAct=EBI-2834493, EBI-1748958;
CC Q9HBU6; O43765: SGTA; NbExp=3; IntAct=EBI-2834493, EBI-347996;
CC Q9HBU6; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2834493, EBI-744081;
CC Q9HBU6; Q86UW2: SLC51B; NbExp=3; IntAct=EBI-2834493, EBI-12266756;
CC Q9HBU6; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2834493, EBI-741480;
CC Q9HBU6; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-2834493, EBI-10173939;
CC Q9HBU6; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2834493, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11044454}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HBU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HBU6-2; Sequence=VSP_047191;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, placenta, heart,
CC leukocyte, ovary and testis. {ECO:0000269|PubMed:11044454}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
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DR EMBL; AF207600; AAF71220.2; -; mRNA.
DR EMBL; AC087241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96479.1; -; Genomic_DNA.
DR EMBL; BC006111; AAH06111.2; -; mRNA.
DR EMBL; BC066907; AAH66907.1; -; mRNA.
DR RefSeq; NP_001034570.1; NM_001039481.1.
DR RefSeq; NP_061108.2; NM_018638.4.
DR AlphaFoldDB; Q9HBU6; -.
DR SMR; Q9HBU6; -.
DR BioGRID; 120680; 22.
DR IntAct; Q9HBU6; 15.
DR STRING; 9606.ENSP00000266517; -.
DR SwissLipids; SLP:000001769; -. [Q9HBU6-1]
DR GlyGen; Q9HBU6; 1 site.
DR iPTMnet; Q9HBU6; -.
DR PhosphoSitePlus; Q9HBU6; -.
DR BioMuta; ETNK1; -.
DR DMDM; 14194724; -.
DR EPD; Q9HBU6; -.
DR jPOST; Q9HBU6; -.
DR MassIVE; Q9HBU6; -.
DR MaxQB; Q9HBU6; -.
DR PaxDb; Q9HBU6; -.
DR PeptideAtlas; Q9HBU6; -.
DR PRIDE; Q9HBU6; -.
DR ProteomicsDB; 33849; -.
DR ProteomicsDB; 81595; -. [Q9HBU6-1]
DR Antibodypedia; 24166; 213 antibodies from 22 providers.
DR DNASU; 55500; -.
DR Ensembl; ENST00000671733.1; ENSP00000500633.1; ENSG00000139163.16. [Q9HBU6-1]
DR Ensembl; ENST00000672951.1; ENSP00000499814.1; ENSG00000139163.16. [Q9HBU6-2]
DR GeneID; 55500; -.
DR KEGG; hsa:55500; -.
DR UCSC; uc001rfs.4; human. [Q9HBU6-1]
DR CTD; 55500; -.
DR DisGeNET; 55500; -.
DR GeneCards; ETNK1; -.
DR HGNC; HGNC:24649; ETNK1.
DR HPA; ENSG00000139163; Low tissue specificity.
DR MIM; 609858; gene.
DR neXtProt; NX_Q9HBU6; -.
DR OpenTargets; ENSG00000139163; -.
DR PharmGKB; PA134921265; -.
DR VEuPathDB; HostDB:ENSG00000139163; -.
DR eggNOG; KOG4720; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR HOGENOM; CLU_012712_1_0_1; -.
DR InParanoid; Q9HBU6; -.
DR OrthoDB; 349250at2759; -.
DR PhylomeDB; Q9HBU6; -.
DR TreeFam; TF313549; -.
DR BioCyc; MetaCyc:HS06586-MON; -.
DR BRENDA; 2.7.1.82; 2681.
DR PathwayCommons; Q9HBU6; -.
DR Reactome; R-HSA-1483213; Synthesis of PE.
DR SignaLink; Q9HBU6; -.
DR UniPathway; UPA00558; UER00741.
DR BioGRID-ORCS; 55500; 36 hits in 1083 CRISPR screens.
DR ChiTaRS; ETNK1; human.
DR GenomeRNAi; 55500; -.
DR Pharos; Q9HBU6; Tbio.
DR PRO; PR:Q9HBU6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9HBU6; protein.
DR Bgee; ENSG00000139163; Expressed in jejunal mucosa and 187 other tissues.
DR ExpressionAtlas; Q9HBU6; baseline and differential.
DR Genevisible; Q9HBU6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004305; F:ethanolamine kinase activity; IDA:UniProtKB.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..452
FT /note="Ethanolamine kinase 1"
FT /id="PRO_0000206227"
FT REGION 26..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 228..452
FT /note="RLIARQLAKIHAIHAHNGWIPKSNLWLKMGKYFSLIPTGFADEDINKRFLSD
FT IPSSQILQEEMTWMKEILSNLGSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYL
FT AYDIGNHFNEFAGVSDVDYSLYPDRELQSQWLRAYLEAYKEFKGFGTEVTEKEVEILFI
FT QVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAIVRFNQYFKMKPEVTALKVPE ->
FT SLSSLTLCKGKTTRCFGLTGCRGSRLLLSFF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047191"
SQ SEQUENCE 452 AA; 50968 MW; 9AF29EAC556ED91F CRC64;
MLCGRPRSSS DNRNFLRERA GLSSAAVQTR IGNSAASRRS PAARPPVPAP PALPRGRPGT
EGSTSLSAPA VLVVAVAVVV VVVSAVAWAM ANYIHVPPGS PEVPKLNVTV QDQEEHRCRE
GALSLLQHLR PHWDPQEVTL QLFTDGITNK LIGCYVGNTM EDVVLVRIYG NKTELLVDRD
EEVKSFRVLQ AHGCAPQLYC TFNNGLCYEF IQGEALDPKH VCNPAIFRLI ARQLAKIHAI
HAHNGWIPKS NLWLKMGKYF SLIPTGFADE DINKRFLSDI PSSQILQEEM TWMKEILSNL
GSPVVLCHND LLCKNIIYNE KQGDVQFIDY EYSGYNYLAY DIGNHFNEFA GVSDVDYSLY
PDRELQSQWL RAYLEAYKEF KGFGTEVTEK EVEILFIQVN QFALASHFFW GLWALIQAKY
STIEFDFLGY AIVRFNQYFK MKPEVTALKV PE
